Research workbench
Structure of V267F mutant HPRK/P
Analyse Structure of V267F mutant HPRK/P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QMH
- Type
- protein
- Length
- 2,010 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hpr KINASE/PHOSPHORYLASE
- EC
- 2.7.11.-, 2.7.4.-
- UniProt
- Q9RE09
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 10 distinct chains · 28% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hpr KINASE/PHOSPHORYLASE (EC 2.7.11.-, 2.7.4.-) | protein | 161 | 26% helix, 34% strand | Q9RE09 |
| B, D | Hpr KINASE/PHOSPHORYLASE (EC 2.7.11.-, 2.7.4.-) | protein | 181 | 29% helix, 34% strand | Q9RE09 |
| C | Hpr KINASE/PHOSPHORYLASE (EC 2.7.11.-, 2.7.4.-) | protein | 164 | 28% helix, 35% strand | Q9RE09 |
| E | Hpr KINASE/PHOSPHORYLASE (EC 2.7.11.-, 2.7.4.-) | protein | 164 | 27% helix, 36% strand | Q9RE09 |
| F | Hpr KINASE/PHOSPHORYLASE (EC 2.7.11.-, 2.7.4.-) | protein | 160 | 29% helix, 35% strand | Q9RE09 |
| G, I | Hpr KINASE/PHOSPHORYLASE (EC 2.7.11.-, 2.7.4.-) | protein | 160 | 26% helix, 35% strand | Q9RE09 |
| H | Hpr KINASE/PHOSPHORYLASE (EC 2.7.11.-, 2.7.4.-) | protein | 178 | 28% helix, 36% strand | Q9RE09 |
| J | Hpr KINASE/PHOSPHORYLASE (EC 2.7.11.-, 2.7.4.-) | protein | 178 | 29% helix, 37% strand | Q9RE09 |
| K | Hpr KINASE/PHOSPHORYLASE (EC 2.7.11.-, 2.7.4.-) | protein | 162 | 26% helix, 36% strand | Q9RE09 |
| L | Hpr KINASE/PHOSPHORYLASE (EC 2.7.11.-, 2.7.4.-) | protein | 161 | 28% helix, 35% strand | Q9RE09 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 337 | 0.82 | 0.92 | 51 | empty |
| 2 | 892 | 0.81 | 0.84 | 95 | empty |
| 3 | 401 | 0.81 | 0.89 | 52 | empty |
| 4 | 303 | 0.80 | 0.91 | 45 | empty |
| 5 | 308 | 0.79 | 0.90 | 44 | empty |
Interfaces
30 interfaces between chains.
- D–F · 1396 Ų buried · 10 hydrogen bonds · protein-protein
- H–I · 1378 Ų buried · 10 hydrogen bonds · protein-protein
- J–L · 1372 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 1308 Ų buried · 8 hydrogen bonds · protein-protein
- G–H · 1022 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 2QMH · structure of V267F mutant HprK/P · the same entry in another collection · chain L against L, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9RE09
- Elsewhere: RCSB PDB 2QMH · PDBe 2QMH · UniProt Q9RE09
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